ID A0A0E3Z086_9GAMM Unreviewed; 379 AA.
AC A0A0E3Z086;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN ORFNames=WQ53_05895 {ECO:0000313|EMBL:AKC86373.1};
OS Pseudoxanthomonas suwonensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=314722 {ECO:0000313|EMBL:AKC86373.1, ECO:0000313|Proteomes:UP000033067};
RN [1] {ECO:0000313|EMBL:AKC86373.1, ECO:0000313|Proteomes:UP000033067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J1 {ECO:0000313|EMBL:AKC86373.1,
RC ECO:0000313|Proteomes:UP000033067};
RX PubMed=26067962;
RA Hou L., Jiang J., Xu Z., Zhou Y., Leung F.C.;
RT "Complete Genome Sequence of Pseudoxanthomonas suwonensis Strain J1, a
RT Cellulose-Degrading Bacterium Isolated from Leaf- and Wood-Enriched Soil.";
RL Genome Announc. 3:e00614-15(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8; Evidence={ECO:0000256|RuleBase:RU361174};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC {ECO:0000256|RuleBase:RU361174}.
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DR EMBL; CP011144; AKC86373.1; -; Genomic_DNA.
DR RefSeq; WP_052631207.1; NZ_CP011144.1.
DR AlphaFoldDB; A0A0E3Z086; -.
DR KEGG; psuw:WQ53_05895; -.
DR PATRIC; fig|314722.6.peg.1251; -.
DR OrthoDB; 9815836at2; -.
DR Proteomes; UP000033067; Chromosome.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR044846; GH10.
DR InterPro; IPR031158; GH10_AS.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31490:SF88; BETA-XYLANASE; 1.
DR PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00591; GH10_1; 1.
DR PROSITE; PS51760; GH10_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU361174};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361174};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361174};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361174};
KW Reference proteome {ECO:0000313|Proteomes:UP000033067};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000313|EMBL:AKC86373.1}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..379
FT /note="Beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002416366"
FT DOMAIN 21..376
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT ACT_SITE 264
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ SEQUENCE 379 AA; 42647 MW; CAF9D6B453906F57 CRC64;
MRTPLLALAA ALALALPAKA ADRPTTLKDA FADAFLLGTA VNDDIVSGRD ARAQALVPLH
FNSITAENVM KAEVINPQPD TWDFAAADAF VAFGEKHGMF IVGHTLVWHN QTPDWFFFGA
DGTPVGREAL AERMRQYIEQ VAGRYTGRVH AWDVVNEVMG EDGQYRPTKW VEGIGDGDEL
VKLAFRFASQ YAPDAELYYN DFNAWRPEKR DGIVRMVRML QDAGIRIDGI GMQGHWGLNY
PATADIEAAI DAYAALGVKV MITELDVDVL PLTREGQIIG QGMAHPQFQL PEFKRFLDPY
PDGLPAEVQK RLADRYAELF RIFHGRRDRI DRVSIWGVHD PMSWKNDYPI PNRTNYPLLF
DRQYRPKPAF DAVLAVPFE
//
